Calabrò Emanuele, Magazù Salvatore
a Department of Mathematics and Informatics Sciences , Physics Sciences and Earth Sciences, University of Messina , Messina , Italy.
Electromagn Biol Med. 2017;36(3):279-288. doi: 10.1080/15368378.2017.1328691. Epub 2017 Jun 20.
The aim of this article was to study the effects of mobile phone electromagnetic waves at 1750 MHz on the Amide I and Amide II vibration bands of some proteins in bidistilled water solution by means of Fourier transform infrared (FTIR) spectroscopy and Fourier self-deconvolution (FSD) analysis. The proteins that were used for the experiment were hemoglobin, myoglobin, bovine serum albumin and lysozyme. The exposure system consisted of microwaves emitted by an operational mobile phone at the frequency at 1750 MHz at the average power density of 1 W/m. Exposed and control samples were analyzed using FTIR spectroscopy and FSD analysis. The main result was that Amide I band of the proteins that were used increased significantly (p < 0.05) after 4 h of exposure to MWs, whereas Amide II band did not change significantly. This result can be explained assuming that the α-helix structure of the proteins aligned itself with the direction of the electromagnetic field due to the alignment of C = O stretching and N - H bending ligands that are oriented along with the α-helix axis that give rise to the Amide I mode.
本文旨在通过傅里叶变换红外（FTIR）光谱和傅里叶自去卷积（FSD）分析，研究1750MHz手机电磁波对双蒸水溶液中某些蛋白质的酰胺I和酰胺II振动带的影响。实验所用蛋白质为血红蛋白、肌红蛋白、牛血清白蛋白和溶菌酶。暴露系统由一部工作在1750MHz频率、平均功率密度为1W/m的手机发射的微波组成。使用FTIR光谱和FSD分析对暴露样品和对照样品进行分析。主要结果是，暴露于微波4小时后，所用蛋白质的酰胺I带显著增加（p<0.05），而酰胺II带没有显著变化。这一结果可以解释为，由于沿α-螺旋轴取向的C=O伸缩和N-H弯曲配体的排列，α-螺旋结构与电磁场方向对齐，从而产生酰胺I模式。
